Crystal structure of TFIID TATA-box binding protein

Dimitar B. Nikolov, Shu Hong Hu, Judith Lin, Alexander Gasch, Alexander Hoffmann, Masami Horikoshi, Nam Hai Chua, Robert G. Roeder, Stephen Burley

Research output: Contribution to journalArticle

283 Citations (Scopus)

Abstract

The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDτ) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 Å resolution. This highly symmetric α/β structure contains a new DMA-binding fold, resembling a molecular 'saddle' that sits astride the DMA. The DNA-binding surface is a curved, antiparallel β-sheet. When bound to DMA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.

Original languageEnglish (US)
Pages (from-to)40-46
Number of pages7
JournalNature
Volume360
Issue number6399
DOIs
StatePublished - Jan 1 1992
Externally publishedYes

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Transcription Factor TFIID
TATA-Box Binding Protein
Peptide Initiation Factors
X Ray Crystallography
Arabidopsis
Transcription Factors
DNA
Proteins
tributyl phosphate

All Science Journal Classification (ASJC) codes

  • General

Cite this

Nikolov, D. B., Hu, S. H., Lin, J., Gasch, A., Hoffmann, A., Horikoshi, M., ... Burley, S. (1992). Crystal structure of TFIID TATA-box binding protein. Nature, 360(6399), 40-46. https://doi.org/10.1038/360040a0
Nikolov, Dimitar B. ; Hu, Shu Hong ; Lin, Judith ; Gasch, Alexander ; Hoffmann, Alexander ; Horikoshi, Masami ; Chua, Nam Hai ; Roeder, Robert G. ; Burley, Stephen. / Crystal structure of TFIID TATA-box binding protein. In: Nature. 1992 ; Vol. 360, No. 6399. pp. 40-46.
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Nikolov, DB, Hu, SH, Lin, J, Gasch, A, Hoffmann, A, Horikoshi, M, Chua, NH, Roeder, RG & Burley, S 1992, 'Crystal structure of TFIID TATA-box binding protein', Nature, vol. 360, no. 6399, pp. 40-46. https://doi.org/10.1038/360040a0

Crystal structure of TFIID TATA-box binding protein. / Nikolov, Dimitar B.; Hu, Shu Hong; Lin, Judith; Gasch, Alexander; Hoffmann, Alexander; Horikoshi, Masami; Chua, Nam Hai; Roeder, Robert G.; Burley, Stephen.

In: Nature, Vol. 360, No. 6399, 01.01.1992, p. 40-46.

Research output: Contribution to journalArticle

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T1 - Crystal structure of TFIID TATA-box binding protein

AU - Nikolov, Dimitar B.

AU - Hu, Shu Hong

AU - Lin, Judith

AU - Gasch, Alexander

AU - Hoffmann, Alexander

AU - Horikoshi, Masami

AU - Chua, Nam Hai

AU - Roeder, Robert G.

AU - Burley, Stephen

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AB - The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDτ) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 Å resolution. This highly symmetric α/β structure contains a new DMA-binding fold, resembling a molecular 'saddle' that sits astride the DMA. The DNA-binding surface is a curved, antiparallel β-sheet. When bound to DMA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.

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Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M et al. Crystal structure of TFIID TATA-box binding protein. Nature. 1992 Jan 1;360(6399):40-46. https://doi.org/10.1038/360040a0